MOLECULAR-CLONING AND EXPRESSION OF AN IL-6 SIGNAL TRANSDUCER, GP130
MOLECULAR-CLONING AND EXPRESSION OF AN IL-6 SIGNAL TRANSDUCER, GP130
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DOI:
10.1016/0092-8674(90)90411-7
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发表时间:
1990-12-21
期刊:
影响因子:
64.5
通讯作者:
KISHIMOTO, T
中科院分区:
文献类型:
--
作者:
HIBI, M;MURAKAMI, M;KISHIMOTO, T
Interleukin-6 (IL-6) signal is transduced through a membrane glycoprotein, gp130, which associates with IL-6 receptor (IL-6-R). A cDNA encoding human gp130 has been cloned, revealing that it consists of 918 amino acids with a single transmembrane domain. The extracellular region comprises six units of a fibronectin type III module, and part of this region of approximately 200 amino acids has features typical of a cytokine receptor family. A cDNA-expressed gp130 showed no binding property to IL-6 or several other cytokines. Although a transfectant with an IL-6-R cDNA expressed mainly low affinity IL-6 binding sites, an increase in high affinity binding sites was observed after cotransfection with a gp130 cDNA. This confirmed that a gp130 is involved in the formation of high affinity IL-6 binding sites. A cloned gp130 could associate with a complex of IL-6 and soluble IL-6-R and transduce the growth signal when expressed in a murine IL-3-dependent growth signal when expressed in a murine IL-3-dependent cell line.